Evidence map›Paper›PMID 28538158›Full record

ArticleBiophysical journal2017

GlnK Facilitates the Dynamic Regulation of Bacterial Nitrogen Assimilation.

Adam Gosztolai, Jörg Schumacher, Volker Behrends, Jacob G Bundy, Franziska Heydenreich, Mark H Bennett, Martin Buck, Mauricio Barahona

Abstract read
In one paragraph

Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

12 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. The Global Response ofFrontiers in microbiology · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors.

Adam GosztolaiDepartment of Mathematics, Imperial College London, London, United Kingdom.
Jörg SchumacherDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Volker BehrendsDepartment of Surgery and Cancer, Imperial College London, London, United Kingdom; Department of Life Sciences, University of Roehampton, London, United Kingdom.
Jacob G BundyDepartment of Surgery and Cancer, Imperial College London, London, United Kingdom.
Franziska HeydenreichDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Mark H BennettDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Martin BuckDepartment of Life Sciences, Imperial College London, London, United Kingdom.
Mauricio BarahonaDepartment of Mathematics, Imperial College London, London, United Kingdom. Electronic address: m.barahona@imperial.ac.uk.

Funding

Biotechnology and Biological Sciences Research Council BB/G020434/1
6 · The paper itself

Abstract

Ammonium assimilation in Escherichia coli is regulated by two paralogous proteins (GlnB and GlnK), which orchestrate interactions with regulators of gene expression, transport proteins, and metabolic pathways. Yet how they conjointly modulate the activity of glutamine synthetase, the key enzyme for nitrogen assimilation, is poorly understood. We combine experiments and theory to study the dynamic roles of GlnB and GlnK during nitrogen starvation and upshift. We measure time-resolved in vivo concentrations of metabolites, total and posttranslationally modified proteins, and develop a concise biochemical model of GlnB and GlnK that incorporates competition for active and allosteric sites, as well as functional sequestration of GlnK. The model predicts the responses of glutamine synthetase, GlnB, and GlnK under time-varying external ammonium level in the wild-type and two genetic knock-outs. Our results show that GlnK is tightly regulated under nitrogen-rich conditions, yet it is expressed during ammonium run-out and starvation. This suggests a role for GlnK as a buffer of nitrogen shock after starvation, and provides a further functional link between nitrogen and carbon metabolisms.

Indexed as

AlgorithmsAmmonium CompoundsCation Transport ProteinsEscherichia coliEscherichia coli ProteinsGene Knockout TechniquesModels, BiologicalNitrogenNucleotidyltransferasesPII Nitrogen Regulatory ProteinsStress, PhysiologicalAmmonium CompoundsAmtB protein, E coliCation Transport ProteinsEscherichia coli ProteinsGlnB protein, E coliglnK protein, E coliNitrogenNucleotidyltransferasesPII Nitrogen Regulatory Proteins

Identifiers

PMID28538158
PMCPMC5448240

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.